| Title : The coding sequence of the hemolytically inactive C4A6 allotype of human complement component C4 reveals that a single arginine to tryptophan substitution at beta-chain residue 458 is the likely cause of the defect - Anderson_1992_J.Immunol_148_2795 |
| Author(s) : Anderson MJ , Milner CM , Cotton RG , Campbell RD |
| Ref : J Immunol , 148 :2795 , 1992 |
| Abstract : |
| PubMedSearch : Anderson_1992_J.Immunol_148_2795 |
| PubMedID: 1573268 |
| Title : The coding sequence of the hemolytically inactive C4A6 allotype of human complement component C4 reveals that a single arginine to tryptophan substitution at beta-chain residue 458 is the likely cause of the defect - Anderson_1992_J.Immunol_148_2795 |
| Author(s) : Anderson MJ , Milner CM , Cotton RG , Campbell RD |
| Ref : J Immunol , 148 :2795 , 1992 |
| Abstract : |
| PubMedSearch : Anderson_1992_J.Immunol_148_2795 |
| PubMedID: 1573268 |
| Title : The coding sequence of the hemolytically inactive C4A6 allotype of human complement component C4 reveals that a single arginine to tryptophan substitution at beta-chain residue 458 is the likely cause of the defect - Anderson_1992_J.Immunol_148_2795 |
| Author(s) : Anderson MJ , Milner CM , Cotton RG , Campbell RD |
| Ref : J Immunol , 148 :2795 , 1992 |
| Abstract : |
| PubMedSearch : Anderson_1992_J.Immunol_148_2795 |
| PubMedID: 1573268 |